Download MendeleyStructure of the cold- and menthol-sensing ion channel TRPM8.
Yin, Y., Wu, M., Zubcevic, L., Borschel, W.F., Lander, G.C., Lee, S.Y.(2018) Science 359: 237-241
- PubMed: 29217583
- DOI: https://doi.org/10.1126/science.aan4325
- Primary Citation of Related Structures:
6BPQ - PubMed Abstract:
Transient receptor potential melastatin (TRPM) cation channels are polymodal sensors that are involved in a variety of physiological processes. Within the TRPM family, member 8 (TRPM8) is the primary cold and menthol sensor in humans. We determined the cryo-electron microscopy structure of the full-length TRPM8 from the collared flycatcher at an overall resolution of ~4.1 ångstroms. Our TRPM8 structure reveals a three-layered architecture. The amino-terminal domain with a fold distinct among known TRP structures, together with the carboxyl-terminal region, forms a large two-layered cytosolic ring that extensively interacts with the transmembrane channel layer. The structure suggests that the menthol-binding site is located within the voltage-sensor-like domain and thus provides a structural glimpse of the design principle of the molecular transducer for cold and menthol sensation.
Organizational Affiliation:
Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.
